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Secreted Glycoprotein from Live Zaire ebolavirus-Infected Cultures: Preparation, Structural and Biophysical Characterization, and Thermodynamic Stability.
- Source :
-
Journal of Infectious Diseases . 11/15/2007 Supplement, Vol. 196 Issue 2, pS220-S231. 12p. 1 Diagram, 1 Chart, 3 Graphs. - Publication Year :
- 2007
-
Abstract
- Milligram quantities of Zaire ebolavirus nonstructural, secreted glycoprotein (sGP) were purified to homogeneity, and this preparation was characterized by an array of biophysical and biochemical experiments. Mass-spectrometry analysis revealed sGP posttranslational modifications and regions susceptible to limited proteolysis. In solution, sGP has an absolute molar mass of 103 kDa, is monodisperse, and folds into a predominantly β-sheet conformation with a distinct tertiary structure. sGP appears to have a unique free-energy landscape that facilitates reversible folding and a strong propensity for disulfide-linked dimeric quaternary structure under a wide range of conditions; the low apparent free energy of conformation transition of sGP (ΔG = 1.7±0.1 kcal/mol) suggests that the molecule is well suited as a thermodynamically facile switch, which would allow it to report on relatively subtle changes in milieu. In addition, a conformational transition at 37°C was detected in thermal denaturing experiments. On the basis of biophysical and biochemical considerations alone, we propose that the property of being a thermodynamically facile switch is an important clue to reveal sGP functionality. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00221899
- Volume :
- 196
- Issue :
- 2
- Database :
- Academic Search Index
- Journal :
- Journal of Infectious Diseases
- Publication Type :
- Academic Journal
- Accession number :
- 28231100
- Full Text :
- https://doi.org/10.1086/520614